Reviewed, UniProtKB/Swiss-Prot Q71XX5 (MURE_LISMF)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
    EC=6.3.2.13
Alternative name(s):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	LMOf2365_2070

Organism

Listeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]

Taxonomic identifier

265669 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP MF_00208
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208
Subcellular location	Cytoplasm By similarity HAMAP MF_00208.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208
Sequence similarities	Belongs to the murCDEF family. MurE subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: EC tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101910
Regions
	Nucleotide binding	108 – 114	7	ATP Potential
	Region	150 – 151	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	407 – 410	4	Meso-diaminopimelate binding By similarity
	Motif	407 – 410	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	149	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	177	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	183	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	185	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	383	1	Meso-diaminopimelate By similarity
	Binding site	458	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	462	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	217	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q71XX5-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 1145D53BF9CD4BFD	FASTA	491	53,979
	10 20 30 40 50 60 MKLNELMQAI PVFTGEASET IEISHIAQDS RKVKPGTLFI CIDGELVDGH QFASRAVELG 70 80 90 100 110 120 AVAIIAEKQL DVSIPVIYVR DSKRAMAMLA DYFYGSPTQA LKLVGITGTN GKTTVSHLVE 130 140 150 160 170 180 QIVRENGEQT GLIGTMYRKI GDQILETKNT TPDSLTLQET FRDMLLSGVS TAVMEVSSHA 190 200 210 220 230 240 LVQGRVYGSD YDVAVFMNLS QDHLDYHHTM EEYANAKSLL FAQLGNSYHT SNPKIAVLNA 250 260 270 280 290 300 DDEESVRMQK ATAAHVITFG IKQQADFKAN NIRITSHGST FDLRTPIGNF TLKIKMIGNF 310 320 330 340 350 360 SVYNVLAAIA TSFALHIPME KAIKTVESIP GVKGRFELVH AGQEFPVIVD YAHTPDGLLN 370 380 390 400 410 420 VLETIAEFAE KRVFVVVGCG GDRDKGKRPQ MAKIAVDYAT NPIFTSDNPR SENPRAIIED 430 440 450 460 470 480 MIQGVPYSDS YVVHENRRDA IRFAVNEAEA GDVILIAGKG HEDYQVIGDE VIDFDDRVEA 490 RIAIEKKLGL A

References

[1]

"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species." Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M. Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017262 Genomic DNA. Translation: AAT04840.1.
RefSeq	YP_014663.1.
3D structure databases
SMR	Q71XX5. Positions 2-486.
ModBase	Search...
Protein-protein interaction databases
STRING	Q71XX5.
Genome annotation databases
GeneID	2797029.
GenomeReviews	Gene locus LMOf2365_2070 in contig AE017262_GR.
KEGG	lmf:LMOf2365_2070.
TIGR	LMOf2365_2070.
Phylogenomic databases
eggNOG	COG0769.
HOGENOM	HBG602753.
OMA	EHLDFHG.
Enzyme and pathway databases
BioCyc	LMON265669:LMOF2365_2070-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_LISMF

Accession

Primary (citable) accession number: Q71XX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)